SitesBLAST
Comparing WP_018232951.1 NCBI__GCF_000378965.1:WP_018232951.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
38% identity, 93% coverage: 30:513/521 of query aligns to 1:485/487 of 1m21A
- active site: K81 (= K109), S160 (= S185), S161 (= S186), T179 (= T204), T181 (= T206), D182 (≠ G207), G183 (≠ N208), S184 (= S209), C187 (≠ G212)
- binding : A129 (= A158), N130 (vs. gap), F131 (= F159), C158 (≠ A183), G159 (= G184), S160 (= S185), S184 (= S209), C187 (≠ G212), I212 (≠ L237), R318 (vs. gap), L321 (≠ F348), L365 (≠ W391), F426 (≠ S451)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 91% coverage: 36:509/521 of query aligns to 6:471/478 of 3h0mA
- active site: K72 (= K109), S147 (= S185), S148 (= S186), S166 (≠ T204), T168 (= T206), G169 (= G207), G170 (≠ N208), S171 (= S209), Q174 (≠ G212)
- binding glutamine: M122 (≠ F159), G123 (≠ S160), D167 (= D205), T168 (= T206), G169 (= G207), G170 (≠ N208), S171 (= S209), F199 (≠ L237), Y302 (≠ F339), R351 (= R387), D418 (≠ N455)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 91% coverage: 36:509/521 of query aligns to 6:471/478 of 3h0lA
- active site: K72 (= K109), S147 (= S185), S148 (= S186), S166 (≠ T204), T168 (= T206), G169 (= G207), G170 (≠ N208), S171 (= S209), Q174 (≠ G212)
- binding asparagine: G123 (≠ S160), S147 (= S185), G169 (= G207), G170 (≠ N208), S171 (= S209), Y302 (≠ F339), R351 (= R387), D418 (≠ N455)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 83% coverage: 80:509/521 of query aligns to 50:479/485 of 2f2aA
- active site: K79 (= K109), S154 (= S185), S155 (= S186), S173 (≠ T204), T175 (= T206), G176 (= G207), G177 (≠ N208), S178 (= S209), Q181 (≠ G212)
- binding glutamine: G130 (≠ S160), S154 (= S185), D174 (= D205), T175 (= T206), G176 (= G207), S178 (= S209), F206 (≠ L237), Y309 (≠ F339), Y310 (≠ E340), R358 (≠ S388), D425 (≠ N456)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 83% coverage: 80:509/521 of query aligns to 50:479/485 of 2dqnA
- active site: K79 (= K109), S154 (= S185), S155 (= S186), S173 (≠ T204), T175 (= T206), G176 (= G207), G177 (≠ N208), S178 (= S209), Q181 (≠ G212)
- binding asparagine: M129 (≠ F159), G130 (≠ S160), T175 (= T206), G176 (= G207), S178 (= S209), Y309 (≠ F339), Y310 (≠ E340), R358 (≠ S388), D425 (≠ N456)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 93% coverage: 34:520/521 of query aligns to 27:503/507 of Q84DC4
- T31 (≠ G38) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K109) mutation to A: Abolishes activity on mandelamide.
- S180 (= S185) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S186) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G207) mutation to A: Increase in KM values for aromatic substrates, but not aliphatic substrates. Active against lactamide but not against mandelamide; when associated with H-207 and E-382.; mutation to V: Increase in KM values for aromatic substrates, but not aliphatic substrates.
- S204 (= S209) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ G212) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with E-382. Active against lactamide but not against mandelamide; when associated with A-202 and E-382. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with S-316 and N-437.
- S316 (≠ E340) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- Q382 (≠ G411) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with H-207. Active against lactamide but not against mandelamide; when associated with A-202 and H-207.
- I437 (= I446) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with I-31. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-316.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
29% identity, 93% coverage: 32:515/521 of query aligns to 2:560/564 of 6te4A
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 90% coverage: 39:507/521 of query aligns to 4:457/468 of 3kfuE
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
25% identity, 84% coverage: 81:516/521 of query aligns to 177:600/607 of Q7XJJ7
- K205 (= K109) mutation to A: Loss of activity.
- SS 281:282 (= SS 185:186) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGNS 206:209) binding substrate
- S305 (= S209) mutation to A: Loss of activity.
- R307 (= R211) mutation to A: Loss of activity.
- S360 (≠ H264) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
25% identity, 84% coverage: 81:516/521 of query aligns to 177:600/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A158), T258 (≠ P161), S281 (= S185), G302 (≠ T206), G303 (= G207), S305 (= S209), S472 (≠ I389), I532 (≠ H453), M539 (≠ I460)
Sites not aligning to the query:
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
25% identity, 84% coverage: 81:516/521 of query aligns to 177:600/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A158), G302 (≠ T206), G303 (= G207), G304 (≠ N208), A305 (≠ S209), V442 (≠ L360), I475 (≠ A392), M539 (≠ I460)
Sites not aligning to the query:
8ey1D Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with n-(3-oxododecanoyl)-l-homoserine lactone
25% identity, 84% coverage: 81:516/521 of query aligns to 177:600/605 of 8ey1D
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 77% coverage: 106:505/521 of query aligns to 92:498/508 of 3a1iA
- active site: K95 (= K109), S170 (= S185), S171 (= S186), G189 (≠ T204), Q191 (≠ T206), G192 (= G207), G193 (≠ N208), A194 (≠ S209), I197 (≠ G212)
- binding benzamide: F145 (= F159), S146 (= S160), G147 (≠ P161), Q191 (≠ T206), G192 (= G207), G193 (≠ N208), A194 (≠ S209), W327 (≠ F337)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 79% coverage: 93:506/521 of query aligns to 75:463/605 of Q936X2
- K91 (= K109) mutation to A: Loss of activity.
- S165 (= S185) mutation to A: Loss of activity.
- S189 (= S209) mutation to A: Loss of activity.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 89% coverage: 35:498/521 of query aligns to 1:442/457 of 6c6gA
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
27% identity, 77% coverage: 100:500/521 of query aligns to 63:434/461 of 4gysB
- active site: K72 (= K109), S146 (= S185), S147 (= S186), T165 (= T204), T167 (= T206), A168 (≠ G207), G169 (≠ N208), S170 (= S209), V173 (≠ G212)
- binding malonate ion: A120 (= A158), G122 (≠ S160), S146 (= S185), T167 (= T206), A168 (≠ G207), S170 (= S209), S193 (≠ H232), G194 (= G233), V195 (≠ I234), R200 (≠ L239), Y297 (≠ S350), R305 (≠ H359)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 45% coverage: 35:271/521 of query aligns to 5:244/457 of 5h6sC
- active site: K77 (= K109), S152 (= S185), S153 (= S186), L173 (≠ T206), G174 (= G207), G175 (≠ N208), S176 (= S209)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A158), R128 (≠ S160), W129 (≠ F162), S152 (= S185), L173 (≠ T206), G174 (= G207), S176 (= S209)
Sites not aligning to the query:
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
31% identity, 31% coverage: 108:269/521 of query aligns to 37:200/450 of 4n0iA
- active site: K38 (= K109), S116 (= S185), S117 (= S186), T135 (= T204), T137 (= T206), G138 (= G207), G139 (≠ N208), S140 (= S209), L143 (≠ G212)
- binding glutamine: G89 (≠ S160), T137 (= T206), G138 (= G207), S140 (= S209), Y168 (≠ L237)
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
26% identity, 89% coverage: 42:504/521 of query aligns to 12:468/482 of 3a2qA
- active site: K69 (= K109), S147 (= S185), S148 (= S186), N166 (≠ T204), A168 (≠ T206), A169 (≠ G207), G170 (≠ N208), A171 (≠ S209), I174 (≠ G212)
- binding 6-aminohexanoic acid: G121 (≠ A158), G121 (≠ A158), N122 (≠ S160), S147 (= S185), A168 (≠ T206), A168 (≠ T206), A169 (≠ G207), A171 (≠ S209), C313 (= C349)
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
34% identity, 29% coverage: 101:253/521 of query aligns to 134:289/579 of Q9TUI8
- S217 (= S185) mutation to A: Loss of activity.
- S218 (= S186) mutation to A: Lowers activity by at least 98%.
- D237 (= D205) mutation D->E,N: Loss of activity.
- S241 (= S209) mutation to A: Loss of activity.
- C249 (≠ L217) mutation to A: Loss of activity.
Query Sequence
>WP_018232951.1 NCBI__GCF_000378965.1:WP_018232951.1
MTHRVLLACLTLILAAPIAWATGDEGGAQFNVVEMTIGEAREGLRSGRFSCRQLTARHLA
RISAYDQAGGLNAIAHINPNAMRRADTLDRAWRDRGEMAPLHCMPVILKDNMHTADMPTE
AGAIALQGFVAAEDAFIVKRLREAGAIVVAKSNMGEWAFSPFHTISSTRGETRNAYDSER
VPAGSSGGTASAIAAAFGIIGLGTDTGNSIRGPAAHLALVGLRPTLGATSRHGIVPLLLN
RDIAGPMTRTVEDAAITFSVIAGHDPADPLTERGKERLREDYRAYLDTGGLSGARLGVMR
ELYQTADADPEVMRIMEQALHDLRDAGAVLVDPFEVFDFEMLRNATGFCSRFRFDLANHL
RDLGDAAPVRTLDEIVSAGRYLAHNERSIAWAMAVDVPPHEMQPPCVDVDGDPRRRALLD
AVLGAMDEQWVDAVIYPTWSNPPRRIGDLDSPHGNNSPVIAPHTGQPAITVPMGFTASGL
PLGLQFLARPFDEHVLFRLAYAYEQHTQHRRPPARFGALSP
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory